CA2197675A1 - Antithrombine iii produite par voie transgenique - Google Patents
Antithrombine iii produite par voie transgeniqueInfo
- Publication number
- CA2197675A1 CA2197675A1 CA002197675A CA2197675A CA2197675A1 CA 2197675 A1 CA2197675 A1 CA 2197675A1 CA 002197675 A CA002197675 A CA 002197675A CA 2197675 A CA2197675 A CA 2197675A CA 2197675 A1 CA2197675 A1 CA 2197675A1
- Authority
- CA
- Canada
- Prior art keywords
- antithrombin iii
- transgenically produced
- atiii
- tgatiii
- monosaccharide composition
- Prior art date
- Legal status (The legal status is an assumption and is not a legal conclusion. Google has not performed a legal analysis and makes no representation as to the accuracy of the status listed.)
- Abandoned
Links
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- BCQZXOMGPXTTIC-UHFFFAOYSA-N halothane Chemical compound FC(F)(F)C(Cl)Br BCQZXOMGPXTTIC-UHFFFAOYSA-N 0.000 description 1
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Classifications
-
- C—CHEMISTRY; METALLURGY
- C07—ORGANIC CHEMISTRY
- C07K—PEPTIDES
- C07K14/00—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof
- C07K14/81—Protease inhibitors
- C07K14/8107—Endopeptidase (E.C. 3.4.21-99) inhibitors
- C07K14/811—Serine protease (E.C. 3.4.21) inhibitors
- C07K14/8121—Serpins
- C07K14/8128—Antithrombin III
-
- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61P—SPECIFIC THERAPEUTIC ACTIVITY OF CHEMICAL COMPOUNDS OR MEDICINAL PREPARATIONS
- A61P31/00—Antiinfectives, i.e. antibiotics, antiseptics, chemotherapeutics
-
- A—HUMAN NECESSITIES
- A01—AGRICULTURE; FORESTRY; ANIMAL HUSBANDRY; HUNTING; TRAPPING; FISHING
- A01K—ANIMAL HUSBANDRY; AVICULTURE; APICULTURE; PISCICULTURE; FISHING; REARING OR BREEDING ANIMALS, NOT OTHERWISE PROVIDED FOR; NEW BREEDS OF ANIMALS
- A01K2217/00—Genetically modified animals
- A01K2217/05—Animals comprising random inserted nucleic acids (transgenic)
-
- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61K—PREPARATIONS FOR MEDICAL, DENTAL OR TOILETRY PURPOSES
- A61K38/00—Medicinal preparations containing peptides
-
- Y—GENERAL TAGGING OF NEW TECHNOLOGICAL DEVELOPMENTS; GENERAL TAGGING OF CROSS-SECTIONAL TECHNOLOGIES SPANNING OVER SEVERAL SECTIONS OF THE IPC; TECHNICAL SUBJECTS COVERED BY FORMER USPC CROSS-REFERENCE ART COLLECTIONS [XRACs] AND DIGESTS
- Y10—TECHNICAL SUBJECTS COVERED BY FORMER USPC
- Y10S—TECHNICAL SUBJECTS COVERED BY FORMER USPC CROSS-REFERENCE ART COLLECTIONS [XRACs] AND DIGESTS
- Y10S530/00—Chemistry: natural resins or derivatives; peptides or proteins; lignins or reaction products thereof
- Y10S530/827—Proteins from mammals or birds
- Y10S530/832—Milk; colostrum
Landscapes
- Health & Medical Sciences (AREA)
- Chemical & Material Sciences (AREA)
- Organic Chemistry (AREA)
- Medicinal Chemistry (AREA)
- General Health & Medical Sciences (AREA)
- Life Sciences & Earth Sciences (AREA)
- Gastroenterology & Hepatology (AREA)
- Biochemistry (AREA)
- Proteomics, Peptides & Aminoacids (AREA)
- Molecular Biology (AREA)
- Genetics & Genomics (AREA)
- Biophysics (AREA)
- Chemical Kinetics & Catalysis (AREA)
- Public Health (AREA)
- Veterinary Medicine (AREA)
- Communicable Diseases (AREA)
- Oncology (AREA)
- Animal Behavior & Ethology (AREA)
- Nuclear Medicine, Radiotherapy & Molecular Imaging (AREA)
- Pharmacology & Pharmacy (AREA)
- General Chemical & Material Sciences (AREA)
- Medicines That Contain Protein Lipid Enzymes And Other Medicines (AREA)
Abstract
L'invention concerne l'antithrombine III humaine produite par voie transgénique (tgATIII). L'ATIII humaine produite par le procédé transgénique de la présente invention présente une composition monosaccharidique comprenant une N-acétylgalactosamine (GalNAc) ainsi que du fucose, une Nacétylglucosamine, du galactose, du mannose, et de l'acide Nacétylneuraminique/acide N-glycolyneuraminique. La composition monosaccharidique diffère de celle du plasma dérivé de ATIII (phATIII). On a découvert que tgATIII présente un coefficient d'épuration accru comparé à phATIII.
Applications Claiming Priority (2)
Application Number | Priority Date | Filing Date | Title |
---|---|---|---|
US08/391,743 | 1995-02-21 | ||
US08/391,743 US5843705A (en) | 1995-02-21 | 1995-02-21 | Transgenically produced antithrombin III |
Publications (1)
Publication Number | Publication Date |
---|---|
CA2197675A1 true CA2197675A1 (fr) | 1996-08-29 |
Family
ID=23547756
Family Applications (1)
Application Number | Title | Priority Date | Filing Date |
---|---|---|---|
CA002197675A Abandoned CA2197675A1 (fr) | 1995-02-21 | 1996-02-21 | Antithrombine iii produite par voie transgenique |
Country Status (5)
Country | Link |
---|---|
US (4) | US5843705A (fr) |
EP (1) | EP0773992A4 (fr) |
AU (1) | AU695249B2 (fr) |
CA (1) | CA2197675A1 (fr) |
WO (1) | WO1996026268A1 (fr) |
Families Citing this family (77)
Publication number | Priority date | Publication date | Assignee | Title |
---|---|---|---|---|
DE122007000007I2 (de) | 1986-04-09 | 2010-12-30 | Genzyme Corp | Genetisch transformierte Tiere, die ein gewünschtes Protein in Milch absondern |
US5843705A (en) * | 1995-02-21 | 1998-12-01 | Genzyme Transgenic Corporation | Transgenically produced antithrombin III |
KR100221124B1 (ko) * | 1996-09-23 | 1999-10-01 | 한상기 | 신규한 카제인 및 그 제조방법 |
US6210736B1 (en) * | 1997-06-17 | 2001-04-03 | Genzyme Transgenics Corporation | Transgenically produced prolactin |
KR20010052345A (ko) | 1998-05-12 | 2001-06-25 | 수잔 씨 복 | 인간 항트롬빈 3 및 그에 관련된 방법 |
US20030005468A1 (en) * | 1998-06-19 | 2003-01-02 | Meade Harry M. | Methods and vectors for improving nucleic acid expression |
CA2343104A1 (fr) * | 1998-09-16 | 2000-03-23 | Nexia Biotechnologies, Inc. | Production de proteines recombinantes dans l'urine |
CA2350233A1 (fr) * | 1998-11-02 | 2000-05-11 | Genzyme Transgenics Corp. | Mammiferes transgeniques et clones |
WO2000025578A2 (fr) * | 1999-04-26 | 2000-05-11 | Trustees Of Tufts College | Procedes de clonage des animaux |
US6580017B1 (en) | 1998-11-02 | 2003-06-17 | Genzyme Transgenics Corporation | Methods of reconstructed goat embryo transfer |
US6781030B1 (en) | 1998-11-02 | 2004-08-24 | Trustee Of Tufts College, Ballou Hall | Methods for cloning mammals using telophase oocytes |
EP1375654A3 (fr) * | 1998-11-02 | 2008-01-16 | GTC Biotherapeutics, Inc. | Mammifères trangéniques et clonés |
EP1818397A1 (fr) * | 1998-11-02 | 2007-08-15 | Trustees Of Tufts College | Procéde pour le clonage des animaux |
EP1958503A3 (fr) | 1999-01-06 | 2008-11-26 | Merrimack Pharmaceuticals, Inc. | Expression d'alpha féto-protéines humaines secrétées dans des animaux transgéniques |
US7208576B2 (en) * | 1999-01-06 | 2007-04-24 | Merrimack Pharmaceuticals, Inc. | Non-glycosylated human alpha-fetoprotein, methods of production, and uses thereof |
EP1914244B1 (fr) | 1999-04-09 | 2013-05-29 | Kyowa Hakko Kirin Co., Ltd. | Procédé pour la modulation de l'activité de molécules immunes fonctionnelles |
EP1194033B1 (fr) * | 1999-05-13 | 2007-12-19 | GTC Biotherapeutics, Inc. | Antithrombine iii produite de maniere transgenique et mutants de celle-ci |
AU782067B2 (en) | 1999-12-20 | 2005-06-30 | Immunex Corporation | TWEAK receptor |
KR100408429B1 (ko) * | 2000-01-24 | 2003-12-06 | 한미약품 주식회사 | 유즙 중에 인간 과립구 콜로니 자극인자를 생산하는형질전환 흑염소 |
US20040205832A1 (en) * | 2000-05-05 | 2004-10-14 | Meade Harry M. | Transgenically produced decorin |
WO2002002793A1 (fr) * | 2000-07-05 | 2002-01-10 | Japan As Represented By Secretary Of Osaka University | Processus de production de glycoproteine |
US6946292B2 (en) | 2000-10-06 | 2005-09-20 | Kyowa Hakko Kogyo Co., Ltd. | Cells producing antibody compositions with increased antibody dependent cytotoxic activity |
US20040226052A1 (en) * | 2000-10-13 | 2004-11-11 | Meade Harry M. | Methods of producing a target molecule in a transgenic animal and purification of the target molecule |
GB0029777D0 (en) * | 2000-12-06 | 2001-01-17 | Regen Therapeutics Plc | Peptides |
CN105131104B (zh) | 2001-10-10 | 2018-11-16 | 诺和诺德公司 | 肽的重构和糖缀合 |
IL164078A0 (en) * | 2002-04-01 | 2005-12-18 | Gtc Biotherapeutics Inc | Treatment of lung disorder |
EP1530629B1 (fr) * | 2002-05-31 | 2011-08-31 | The University of Utah Research Foundation | Variants d'antithrombine iii |
US20040172667A1 (en) * | 2002-06-26 | 2004-09-02 | Cooper Richard K. | Administration of transposon-based vectors to reproductive organs |
US7527966B2 (en) * | 2002-06-26 | 2009-05-05 | Transgenrx, Inc. | Gene regulation in transgenic animals using a transposon-based vector |
US7612250B2 (en) | 2002-07-29 | 2009-11-03 | Trustees Of Tufts College | Nuclear transfer embryo formation method |
WO2004026427A2 (fr) * | 2002-09-17 | 2004-04-01 | Gtc Biotherapeutics, Inc. | Isolement de molecules d'immunoglobuline auxquelles il manque des liaisons disulfure entre les chaines lourdes |
EP2338333B1 (fr) | 2003-04-09 | 2017-09-06 | ratiopharm GmbH | Méthode de glycopegylation et proteines/peptides produits au moyen de ces méthodes |
CN1871252A (zh) * | 2003-09-05 | 2006-11-29 | Gtc生物治疗学公司 | 在转基因哺乳动物奶中生产融合蛋白的方法 |
WO2005035563A1 (fr) | 2003-10-09 | 2005-04-21 | Kyowa Hakko Kogyo Co., Ltd. | Procede de production d'une composition d'antithrombine iii |
US7691810B2 (en) | 2003-10-09 | 2010-04-06 | Kyowa Hakko Kirin Co., Ltd | Method of producing recombinant antithrombin III composition |
WO2005062881A2 (fr) | 2003-12-24 | 2005-07-14 | Transgenrx, Inc. | Therapie genique faisant intervenir des vecteurs de transposon |
EP1725868A4 (fr) * | 2004-01-09 | 2008-02-06 | Univ Utah Res Found | Procedes d'utilisation de variants de atiii a affinite elevee |
US20050169908A1 (en) * | 2004-01-23 | 2005-08-04 | Kazunori Murakami | Use of aerosolized antithrombin to treat acute lung injury |
US20050186608A1 (en) * | 2004-02-19 | 2005-08-25 | Olsen Byron V. | Method for the production of transgenic proteins useful in the treatment of obesity and diabetes |
US20050192226A1 (en) * | 2004-02-20 | 2005-09-01 | Perenlei Enkhbaatar | Method of preventing fibrin clots in pulmonary tissue through the use of aerosolized anticoagulants |
US20050197496A1 (en) * | 2004-03-04 | 2005-09-08 | Gtc Biotherapeutics, Inc. | Methods of protein fractionation using high performance tangential flow filtration |
US20050245444A1 (en) * | 2004-04-30 | 2005-11-03 | Yann Echelard | Method of using recombinant human antithrombin for neurocognitive disorders |
WO2006057466A1 (fr) * | 2004-11-23 | 2006-06-01 | Korea Research Institute Of Bioscience And Biotechnology | Vecteur ciblant le gene de la beta-caseine au moyen d'une recombinaison homologue |
US20060121004A1 (en) * | 2004-12-07 | 2006-06-08 | Yann Echelard | Methods of reducing the incidence of rejection in tissue transplantation through the use of recombinant human antithrombin |
US20060130159A1 (en) * | 2004-12-09 | 2006-06-15 | Nick Masiello | Method of purifying recombinant MSP 1-42 derived from Plasmodium falciparum |
US7531632B2 (en) * | 2006-02-16 | 2009-05-12 | Gtc Biotherapeutics, Inc. | Clarification of transgenic milk using depth filtration |
JP2010521135A (ja) * | 2006-10-06 | 2010-06-24 | セルタクシス,インコーポレイテッド | 細胞の化学忌避 |
US20100205678A1 (en) * | 2007-01-05 | 2010-08-12 | Overstrom Eric W | Oocyte spindle-associated factors improve somatic cell cloning |
US7763281B2 (en) * | 2007-09-17 | 2010-07-27 | Da-Yeh University | Antihypertensive peptide and use thereof |
US9150880B2 (en) * | 2008-09-25 | 2015-10-06 | Proteovec Holding, L.L.C. | Vectors for production of antibodies |
US9157097B2 (en) * | 2008-09-25 | 2015-10-13 | Proteovec Holding, L.L.C. | Vectors for production of growth hormone |
EP2342224A2 (fr) * | 2008-09-25 | 2011-07-13 | TransGenRx, Inc. | Nouveaux vecteurs pour la production d'interféron |
WO2010118360A1 (fr) * | 2009-04-09 | 2010-10-14 | The Board Of Supervisors Of Louisiana State University And Agricultural And Mechanical College | Production de protéines au moyen de vecteurs à base de transposon |
US20110082083A1 (en) * | 2009-04-10 | 2011-04-07 | Gtc Biotherapeutics, Inc. | Formulations of liquid stable antithrombin |
US20100304873A1 (en) * | 2009-05-28 | 2010-12-02 | Lipa Markowitz | Bowling Ball and Football Game Controller |
TR201809898T4 (tr) | 2009-11-03 | 2018-07-23 | Grifols Therapeutics Llc | Alfa-1 protei̇naz i̇nhi̇bi̇törüne yöneli̇k bi̇leşi̇m, yöntem ve ki̇t. |
RU2540480C2 (ru) | 2009-11-24 | 2015-02-10 | Грифольс Терапьютикс Инк. | Способы, композиции и наборы для лиофилизации |
ES2811526T3 (es) | 2010-12-30 | 2021-03-12 | Lab Francais Du Fractionnement | Glicoles como agentes de inactivación de patógenos |
ES2942483T3 (es) | 2011-10-05 | 2023-06-01 | Oned Mat Inc | Materiales activos de nanoestructuras de silicio para baterías de iones de litio y procesos, composiciones, componentes y dispositivos relacionados con los mismos |
TW201400499A (zh) * | 2012-03-12 | 2014-01-01 | Revo Biolog Inc | 抗凝血酶用於治療妊娠毒血症之用途 |
JP6389172B2 (ja) | 2012-08-03 | 2018-09-12 | エルエフビー ユーエスエー インコーポレイテッドLfb Usa, Inc. | 体外式膜型人工肺におけるアンチトロンビンの使用 |
US20160185847A1 (en) | 2012-12-17 | 2016-06-30 | Laboratoire Francais Du Fractionnement Et Des Biotechnologies | Use of monoclonal antibodies for the treatment of inflammation and bacterial infections |
MX2015010428A (es) | 2013-02-13 | 2016-04-13 | Lab Francais Du Fractionnement | Anticuerpos anti-her2 altamente galactosilados y sus usos. |
MX2015010427A (es) | 2013-02-13 | 2016-03-17 | Lab Francais Du Fractionnement | Anticuerpos anti-tnf-alfa altamente galactosilados y sus usos. |
US10034921B2 (en) | 2013-02-13 | 2018-07-31 | Laboratoire Français Du Fractionnement Et Des Biotechnologies | Proteins with modified glycosylation and methods of production thereof |
US10611826B2 (en) | 2013-07-05 | 2020-04-07 | Laboratoire Français Du Fractionnement Et Des Biotechnologies | Affinity chromatography matrix |
CN106573973A (zh) | 2014-06-02 | 2017-04-19 | 法国化学与生物科技实验室 | Fc片段的产生 |
FR3038517B1 (fr) | 2015-07-06 | 2020-02-28 | Laboratoire Francais Du Fractionnement Et Des Biotechnologies | Utilisation de fragments fc modifies en immunotherapie |
US11377687B2 (en) | 2015-10-16 | 2022-07-05 | Inguran, Llc | Methods of genomic evaluation in livestock |
EP3362578B1 (fr) | 2015-10-16 | 2020-08-12 | Inguran, LLC | Méthodes d'évaluation génomique du bétail |
WO2017149391A1 (fr) | 2016-03-02 | 2017-09-08 | Laboratoire Francais Du Fractionnement Et Des Biotechnologies | Utilisation d'antithrombine pour le revêtement d'organes lors d'une transplantation |
FR3060395B1 (fr) | 2016-12-16 | 2019-05-24 | Laboratoire Francais Du Fractionnement Et Des Biotechnologies | Combinaison d'anticorps anti-cd303 et anti-her2 |
DK3385394T3 (da) | 2017-04-07 | 2022-03-07 | Inguran Llc | Fremgangsmåder til genomisk vurdering hos husdyr |
WO2019116096A1 (fr) | 2017-12-15 | 2019-06-20 | Laboratoire Francais Du Fractionnement Et Des Biotechnologies | Production de fragments fc |
CA3095040A1 (fr) * | 2018-04-06 | 2019-10-10 | Camp4 Therapeutics Corporation | Traitement de maladies par modulation ciblee de reseaux de signalisation genique |
EP3581203A1 (fr) | 2018-06-11 | 2019-12-18 | Laboratoire Français du Fractionnement et des Biotechnologies | Anticorps avec activité accrue dans le tractus digestif |
WO2020053661A1 (fr) | 2018-09-13 | 2020-03-19 | Laboratoire Francais Du Fractionnement Et Des Biotechnologies | Procédés de purification d'anticorps émanant du lait de mammifères non humains transgéniques comprenant l'utilisation de chitosane |
Family Cites Families (6)
Publication number | Priority date | Publication date | Assignee | Title |
---|---|---|---|---|
US4517294A (en) * | 1982-03-03 | 1985-05-14 | Genentech, Inc. | Human antithrombin III |
US4632981A (en) * | 1982-07-30 | 1986-12-30 | Genentech, Inc. | Human antithrombin III |
US5366894A (en) * | 1986-06-30 | 1994-11-22 | Pharmaceutical Proteins Limited | Peptide production |
US4873316A (en) * | 1987-06-23 | 1989-10-10 | Biogen, Inc. | Isolation of exogenous recombinant proteins from the milk of transgenic mammals |
DE4028800A1 (de) * | 1990-09-11 | 1992-03-12 | Behringwerke Ag | Gentechnische sialylierung von glykoproteinen |
US5843705A (en) * | 1995-02-21 | 1998-12-01 | Genzyme Transgenic Corporation | Transgenically produced antithrombin III |
-
1995
- 1995-02-21 US US08/391,743 patent/US5843705A/en not_active Expired - Lifetime
-
1996
- 1996-02-21 WO PCT/US1996/002420 patent/WO1996026268A1/fr not_active Application Discontinuation
- 1996-02-21 CA CA002197675A patent/CA2197675A1/fr not_active Abandoned
- 1996-02-21 AU AU50262/96A patent/AU695249B2/en not_active Expired
- 1996-02-21 EP EP96907093A patent/EP0773992A4/fr not_active Ceased
-
1998
- 1998-08-28 US US09/143,155 patent/US6441145B1/en not_active Expired - Lifetime
-
2002
- 2002-07-02 US US10/188,658 patent/US7019193B2/en not_active Expired - Fee Related
-
2005
- 2005-11-14 US US11/284,585 patent/US7928064B2/en not_active Expired - Fee Related
Also Published As
Publication number | Publication date |
---|---|
US7928064B2 (en) | 2011-04-19 |
WO1996026268A1 (fr) | 1996-08-29 |
EP0773992A4 (fr) | 1999-11-03 |
US7019193B2 (en) | 2006-03-28 |
AU695249B2 (en) | 1998-08-13 |
US20080176786A1 (en) | 2008-07-24 |
US20030096974A1 (en) | 2003-05-22 |
US6441145B1 (en) | 2002-08-27 |
US5843705A (en) | 1998-12-01 |
AU5026296A (en) | 1996-09-11 |
EP0773992A1 (fr) | 1997-05-21 |
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Legal Events
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EEER | Examination request | ||
FZDE | Discontinued |